ID   Q2W2T2_MAGSA            Unreviewed;       583 AA.
AC   Q2W2T2;
DT   10-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   10-JAN-2006, sequence version 1.
DT   27-MAR-2024, entry version 89.
DE   RecName: Full=Guanylate cyclase domain-containing protein {ECO:0000259|PROSITE:PS50125};
GN   OrderedLocusNames=amb3039 {ECO:0000313|EMBL:BAE51843.1};
OS   Magnetospirillum magneticum (strain AMB-1 / ATCC 700264).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Magnetospirillaceae; Paramagnetospirillum.
OX   NCBI_TaxID=342108 {ECO:0000313|EMBL:BAE51843.1, ECO:0000313|Proteomes:UP000007058};
RN   [1] {ECO:0000313|EMBL:BAE51843.1, ECO:0000313|Proteomes:UP000007058}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AMB-1 / ATCC 700264 {ECO:0000313|Proteomes:UP000007058};
RX   PubMed=16303747; DOI=10.1093/dnares/dsi002;
RA   Matsunaga T., Okamura Y., Fukuda Y., Wahyudi A.T., Murase Y., Takeyama H.;
RT   "Complete genome sequence of the facultative anaerobic magnetotactic
RT   bacterium Magnetospirillum sp. strain AMB-1.";
RL   DNA Res. 12:157-166(2005).
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DR   EMBL; AP007255; BAE51843.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q2W2T2; -.
DR   STRING; 342108.amb3039; -.
DR   KEGG; mag:amb3039; -.
DR   HOGENOM; CLU_467559_0_0_5; -.
DR   OrthoDB; 7374210at2; -.
DR   Proteomes; UP000007058; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004016; F:adenylate cyclase activity; IEA:UniProt.
DR   GO; GO:0009190; P:cyclic nucleotide biosynthetic process; IEA:InterPro.
DR   GO; GO:0035556; P:intracellular signal transduction; IEA:InterPro.
DR   CDD; cd07302; CHD; 1.
DR   Gene3D; 3.30.70.1230; Nucleotide cyclase; 1.
DR   InterPro; IPR001054; A/G_cyclase.
DR   InterPro; IPR029787; Nucleotide_cyclase.
DR   PANTHER; PTHR43081; ADENYLATE CYCLASE, TERMINAL-DIFFERENTIATION SPECIFIC-RELATED; 1.
DR   PANTHER; PTHR43081:SF1; PH-SENSITIVE ADENYLATE CYCLASE RV1264; 1.
DR   Pfam; PF00211; Guanylate_cyc; 1.
DR   SMART; SM00044; CYCc; 1.
DR   SUPFAM; SSF55073; Nucleotide cyclase; 1.
DR   PROSITE; PS50125; GUANYLATE_CYCLASE_2; 1.
PE   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000007058};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        135..158
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        170..191
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          422..536
FT                   /note="Guanylate cyclase"
FT                   /evidence="ECO:0000259|PROSITE:PS50125"
FT   REGION          77..103
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          237..272
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        238..252
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        253..269
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   583 AA;  62734 MW;  2E553E62101C957B CRC64;
     MIIVHFEVYV MEGRGWMLHA RFPRLERDEA VREAKELEST LGVRTKVLRE TYNTDSNVFD
     EVEVYLSGHN IQPRKSVAAV GGGGGGGTGG KGGGKDSGKG GAAKAGAARK AAGSARARAN
     GPEIGAGAAI LRLTVILLVA AGVGLGVLRL VPSAIVILYD FGFRITPDEY GQMLIIVFGL
     VFLMTAVPLG LRFMPRNANI QFNNARAAAP PPRPQPSEAV KKSLNKLAKK AEAEMIPETW
     GDDPEPEPEP EPPPPPEETP PPQPPPVEEP SAAAAAVDAI PATPAFETTR KVTDRFVDKS
     MQVVRQVAPS TDKYTTFGLN LFMAGAVQAI ARTQKLDSAG QRKLLKTIIE KLGTPGDLAA
     AFYDKVPEYM GEQRYARMFE SGKSAMESWA EGDEGTPMIK LQTSLKDWNK PATEKKQPSL
     MTVMFTDMVG STDLTQARGD QAAQEIVRKH NAIVRTALTQ FAGREVKHTG DGIMASFASA
     ANAVEATVQI QRQVTAHNEK QPNLPLHLRI GLNAGEPIQE EDDLFGSTVQ LAARVCAATD
     SDQTLCTQVV KDLAGGTGAF TDGGMHALKG FRDKFQLWEV LWR
//